IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v14y2023i1d10.1038_s41467-023-40210-3.html
   My bibliography  Save this article

Zinc-finger BED domains drive the formation of the active Hermes transpososome by asymmetric DNA binding

Author

Listed:
  • Laurie Lannes

    (National Institutes of Health)

  • Christopher M. Furman

    (National Institutes of Health)

  • Alison B. Hickman

    (National Institutes of Health)

  • Fred Dyda

    (National Institutes of Health)

Abstract

The Hermes DNA transposon is a member of the eukaryotic hAT superfamily, and its transposase forms a ring-shaped tetramer of dimers. Our investigation, combining biochemical, crystallography and cryo-electron microscopy, and in-cell assays, shows that the full-length Hermes octamer extensively interacts with its transposon left-end through multiple BED domains of three Hermes protomers contributed by three dimers explaining the role of the unusual higher-order assembly. By contrast, the right-end is bound to no BED domains at all. Thus, this work supports a model in which Hermes multimerizes to gather enough BED domains to find its left-end among the abundant genomic DNA, facilitating the subsequent interaction with the right-end.

Suggested Citation

  • Laurie Lannes & Christopher M. Furman & Alison B. Hickman & Fred Dyda, 2023. "Zinc-finger BED domains drive the formation of the active Hermes transpososome by asymmetric DNA binding," Nature Communications, Nature, vol. 14(1), pages 1-18, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-40210-3
    DOI: 10.1038/s41467-023-40210-3
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-023-40210-3
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-023-40210-3?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    References listed on IDEAS

    as
    1. Christian Biémont & Cristina Vieira, 2006. "Junk DNA as an evolutionary force," Nature, Nature, vol. 443(7111), pages 521-524, October.
    2. Sherwin P. Montaño & Ying Z. Pigli & Phoebe A. Rice, 2012. "The Mu transpososome structure sheds light on DDE recombinase evolution," Nature, Nature, vol. 491(7424), pages 413-417, November.
    3. Ivana Grabundzija & Alison B. Hickman & Fred Dyda, 2018. "Helraiser intermediates provide insight into the mechanism of eukaryotic replicative transposition," Nature Communications, Nature, vol. 9(1), pages 1-14, December.
    4. Liqin Zhou & Rupak Mitra & Peter W. Atkinson & Alison Burgess Hickman & Fred Dyda & Nancy L. Craig, 2004. "Transposition of hAT elements links transposable elements and V(D)J recombination," Nature, Nature, vol. 432(7020), pages 995-1001, December.
    5. Chang Liu & Yang Yang & David G. Schatz, 2019. "Structures of a RAG-like transposase during cut-and-paste transposition," Nature, Nature, vol. 575(7783), pages 540-544, November.
    Full references (including those not matched with items on IDEAS)

    Most related items

    These are the items that most often cite the same works as this one and are cited by the same works as this one.
    1. Alexander V. Shkumatov & Nicolas Aryanpour & Cédric A. Oger & Gérôme Goossens & Bernard F. Hallet & Rouslan G. Efremov, 2022. "Structural insight into Tn3 family transposition mechanism," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    2. Christian Parisod & Corinne Mhiri & K Yoong Lim & James J Clarkson & Mark W Chase & Andrew R Leitch & Marie-Angèle Grandbastien, 2012. "Differential Dynamics of Transposable Elements during Long-Term Diploidization of Nicotiana Section Repandae (Solanaceae) Allopolyploid Genomes," PLOS ONE, Public Library of Science, vol. 7(11), pages 1-12, November.
    3. Mercedes Spínola-Amilibia & Lidia Araújo-Bazán & Álvaro Gándara & James M. Berger & Ernesto Arias-Palomo, 2023. "IS21 family transposase cleaved donor complex traps two right-handed superhelical crossings," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    4. Francisco Tenjo-Castaño & Nicholas Sofos & Blanca López-Méndez & Luisa S. Stutzke & Anders Fuglsang & Stefano Stella & Guillermo Montoya, 2022. "Structure of the TnsB transposase-DNA complex of type V-K CRISPR-associated transposon," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    5. Amrit Tiwana & Hani Safadi, 2024. "Atrophy in Aging Systems: Evidence, Dynamics, and Antidote," Information Systems Research, INFORMS, vol. 35(1), pages 66-86, March.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-40210-3. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    If CitEc recognized a bibliographic reference but did not link an item in RePEc to it, you can help with this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.